ID VMP1_HUMAN Reviewed; 406 AA. AC Q96GC9; B4DVV9; Q9H0P4; Q9P089; DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 12-AUG-2020, entry version 146. DE RecName: Full=Vacuole membrane protein 1; DE AltName: Full=Transmembrane protein 49; GN Name=VMP1; Synonyms=TDC1, TMEM49; ORFNames=HSPC292; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Wu G., Couch F.J.; RT "Gene Tdc1 is a transmembrane domain containing gene that amplified and RT overexpressed in human breast cancer."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Yamazaki S., Muta T., Takeshige K.; RT "A novel lipopolysaccharide-inducible gene (#25)."; RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Kidney; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Spleen; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Ovary; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 243-406 (ISOFORM 1). RC TISSUE=Blood; RA Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L., RA Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.; RT "Human partial CDS from CD34+ stem cells."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [9] RP FUNCTION, INTERACTION WITH TJP1, AND SUBCELLULAR LOCATION. RX PubMed=17724469; DOI=10.1038/sj.onc.1210743; RA Sauermann M., Sahin O., Sultmann H., Hahne F., Blaszkiewicz S., Majety M., RA Zatloukal K., Fuzesi L., Poustka A., Wiemann S., Arlt D.; RT "Reduced expression of vacuole membrane protein 1 affects the invasion RT capacity of tumor cells."; RL Oncogene 27:1320-1326(2008). RN [10] RP INTERACTION WITH TP53INP2. RX PubMed=19056683; DOI=10.1091/mbc.e08-07-0671; RA Nowak J., Archange C., Tardivel-Lacombe J., Pontarotti P., Pebusque M.J., RA Vaccaro M.I., Velasco G., Dagorn J.C., Iovanna J.L.; RT "The TP53INP2 protein is required for autophagy in mammalian cells."; RL Mol. Biol. Cell 20:870-881(2009). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [12] RP FUNCTION, INTERACTION WITH TMEM41B, AND REGION VTT DOMAIN. RX PubMed=30093494; DOI=10.1083/jcb.201804132; RA Morita K., Hama Y., Izume T., Tamura N., Ueno T., Yamashita Y., RA Sakamaki Y., Mimura K., Morishita H., Shihoya W., Nureki O., Mano H., RA Mizushima N.; RT "Genome-wide CRISPR screen identifies TMEM41B as a gene required for RT autophagosome formation."; RL J. Cell Biol. 217:3817-3828(2018). RN [13] RP FUNCTION. RX PubMed=30933966; DOI=10.1371/journal.pbio.2007044; RA Shoemaker C.J., Huang T.Q., Weir N.R., Polyakov N.J., Schultz S.W., RA Denic V.; RT "CRISPR screening using an expanded toolkit of autophagy reporters RT identifies TMEM41B as a novel autophagy factor."; RL PLoS Biol. 17:E2007044-E2007044(2019). CC -!- FUNCTION: Stress-induced protein that, when overexpressed, promotes CC formation of intracellular vacuoles followed by cell death. May be CC involved in the cytoplasmic vacuolization of acinar cells during the CC early stage of acute pancreatitis. Plays a role in the initial stages CC of the autophagic process through its interaction with BECN1 (By CC similarity). Involved in cell-cell adhesion. Plays an essential role in CC formation of cell junctions (PubMed:17724469). Required for CC autophagosome formation (PubMed:30093494, PubMed:30933966). CC {ECO:0000250|UniProtKB:Q91ZQ0, ECO:0000269|PubMed:17724469, CC ECO:0000269|PubMed:30093494, ECO:0000269|PubMed:30933966}. CC -!- SUBUNIT: Interacts with BECN1 (By similarity). Interacts with TJP1 CC (PubMed:17724469). Interacts with TP53INP2 (PubMed:19056683). Interacts CC with TMEM41B (PubMed:30093494). {ECO:0000250|UniProtKB:Q91ZQ0, CC ECO:0000269|PubMed:17724469, ECO:0000269|PubMed:19056683, CC ECO:0000269|PubMed:30093494}. CC -!- INTERACTION: CC Q96GC9; Q14457: BECN1; NbExp=3; IntAct=EBI-2800296, EBI-949378; CC Q96GC9; P00387: CYB5R3; NbExp=3; IntAct=EBI-2800296, EBI-1046040; CC Q96GC9; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-2800296, EBI-781551; CC Q96GC9; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-2800296, EBI-18304435; CC Q96GC9; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2800296, EBI-16439278; CC Q96GC9; Q9NUM3: SLC39A9; NbExp=3; IntAct=EBI-2800296, EBI-2823239; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate CC compartment membrane {ECO:0000250|UniProtKB:Q91ZQ0}; Multi-pass CC membrane protein {ECO:0000255}. Cell membrane CC {ECO:0000269|PubMed:17724469}; Multi-pass membrane protein CC {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:Q91ZQ0}; Multi- CC pass membrane protein {ECO:0000255}. Endoplasmic reticulum CC {ECO:0000269|PubMed:17724469}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q96GC9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96GC9-2; Sequence=VSP_056106; CC -!- DOMAIN: The VTT domain was previously called the SNARE-assoc domain. As CC there is no evidence that this domain associates with SNARE proteins, CC it was renamed as VMP1, TMEM41, and TVP38 (VTT) domain. CC {ECO:0000305|PubMed:30093494}. CC -!- SIMILARITY: Belongs to the VMP1 family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/VMP1ID50079ch17q23.html"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF214006; AAL36461.1; -; mRNA. DR EMBL; AB047551; BAF47368.1; -; mRNA. DR EMBL; AL136711; CAB66646.1; -; mRNA. DR EMBL; AK301254; BAG62821.1; -; mRNA. DR EMBL; CR533521; CAG38552.1; -; mRNA. DR EMBL; AC004686; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC025858; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC040904; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC091271; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC009758; AAH09758.1; -; mRNA. DR EMBL; AF161410; AAF28970.1; -; mRNA. DR CCDS; CCDS11619.1; -. [Q96GC9-1] DR RefSeq; NP_001316323.1; NM_001329394.1. [Q96GC9-1] DR RefSeq; NP_001316326.1; NM_001329397.1. DR RefSeq; NP_001316331.1; NM_001329402.1. [Q96GC9-2] DR RefSeq; NP_112200.2; NM_030938.4. [Q96GC9-1] DR BioGRID; 123567; 122. DR IntAct; Q96GC9; 108. DR MINT; Q96GC9; -. DR STRING; 9606.ENSP00000262291; -. DR TCDB; 8.A.97.1.1; the epg-3/vmp1 (epg/vpm) family. DR iPTMnet; Q96GC9; -. DR PhosphoSitePlus; Q96GC9; -. DR SwissPalm; Q96GC9; -. DR BioMuta; VMP1; -. DR DMDM; 74731809; -. DR EPD; Q96GC9; -. DR jPOST; Q96GC9; -. DR MassIVE; Q96GC9; -. DR MaxQB; Q96GC9; -. DR PaxDb; Q96GC9; -. DR PeptideAtlas; Q96GC9; -. DR PRIDE; Q96GC9; -. DR ProteomicsDB; 5298; -. DR ProteomicsDB; 76615; -. [Q96GC9-1] DR TopDownProteomics; Q96GC9-1; -. [Q96GC9-1] DR Antibodypedia; 31116; 256 antibodies. DR DNASU; 81671; -. DR Ensembl; ENST00000262291; ENSP00000262291; ENSG00000062716. [Q96GC9-1] DR GeneID; 81671; -. DR KEGG; hsa:81671; -. DR UCSC; uc002ixu.5; human. [Q96GC9-1] DR CTD; 81671; -. DR DisGeNET; 81671; -. DR EuPathDB; HostDB:ENSG00000062716.10; -. DR GeneCards; VMP1; -. DR HGNC; HGNC:29559; VMP1. DR HPA; ENSG00000062716; Tissue enriched (blood). DR MIM; 611753; gene. DR neXtProt; NX_Q96GC9; -. DR OpenTargets; ENSG00000062716; -. DR PharmGKB; PA142670765; -. DR eggNOG; KOG1109; Eukaryota. DR GeneTree; ENSGT00390000007230; -. DR HOGENOM; CLU_033298_0_1_1; -. DR InParanoid; Q96GC9; -. DR KO; K21248; -. DR OMA; KRVPNIW; -. DR PhylomeDB; Q96GC9; -. DR TreeFam; TF313699; -. DR PathwayCommons; Q96GC9; -. DR BioGRID-ORCS; 81671; 597 hits in 871 CRISPR screens. DR ChiTaRS; VMP1; human. DR GeneWiki; TMEM49; -. DR GenomeRNAi; 81671; -. DR Pharos; Q96GC9; Tbio. DR PRO; PR:Q96GC9; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q96GC9; protein. DR Bgee; ENSG00000062716; Expressed in left coronary artery and 240 other tissues. DR ExpressionAtlas; Q96GC9; baseline and differential. DR Genevisible; Q96GC9; HS. DR GO; GO:0000421; C:autophagosome membrane; ISS:UniProtKB. DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0000407; C:phagophore assembly site; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000045; P:autophagosome assembly; IMP:UniProtKB. DR GO; GO:0006914; P:autophagy; IBA:GO_Central. DR GO; GO:0034329; P:cell junction assembly; IMP:UniProtKB. DR GO; GO:0098609; P:cell-cell adhesion; IMP:UniProtKB. DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl. DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central. DR InterPro; IPR032816; SNARE_assoc. DR Pfam; PF09335; SNARE_assoc; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Autophagy; Cell adhesion; Cell membrane; KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Vacuole. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000244|PubMed:22814378" FT CHAIN 2..406 FT /note="Vacuole membrane protein 1" FT /id="PRO_0000284546" FT TOPO_DOM 2..43 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 44..64 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 65..77 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 78..98 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 99..109 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 110..130 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 131..250 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 251..271 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 272..273 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 274..294 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 295..305 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 306..326 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 327..363 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 364..384 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 385..406 FT /note="Extracellular" FT /evidence="ECO:0000255" FT REGION 173..316 FT /note="VTT domain" FT /evidence="ECO:0000305|PubMed:30093494" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000244|PubMed:22814378" FT VAR_SEQ 1..192 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056106" FT CONFLICT 179 FT /note="S -> F (in Ref. 3; CAB66646 and 5; CAG38552)" FT /evidence="ECO:0000305" SQ SEQUENCE 406 AA; 46238 MW; E9DDE63F80143091 CRC64; MAENGKNCDQ RRVAMNKEHH NGNFTDPSSV NEKKRREREE RQNIVLWRQP LITLQYFSLE ILVILKEWTS KLWHRQSIVV SFLLLLAVLI ATYYVEGVHQ QYVQRIEKQF LLYAYWIGLG ILSSVGLGTG LHTFLLYLGP HIASVTLAAY ECNSVNFPEP PYPDQIICPD EEGTEGTISL WSIISKVRIE ACMWGIGTAI GELPPYFMAR AARLSGAEPD DEEYQEFEEM LEHAESAQDF ASRAKLAVQK LVQKVGFFGI LACASIPNPL FDLAGITCGH FLVPFWTFFG ATLIGKAIIK MHIQKIFVII TFSKHIVEQM VAFIGAVPGI GPSLQKPFQE YLEAQRQKLH HKSEMGTPQG ENWLSWMFEK LVVVMVCYFI LSIINSMAQS YAKRIQQRLN SEEKTK //